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• W1991768142 abstract "Resonance Raman spectra of cytochrome c oxidase in intact whole mitochondria were selectively observed. The Raman bands observed at 576, 517, and 369 cm-1 for the carbon monoxide-bound state were assigned to the δFe–C–O, νFe–CO, and δFe–C–O modes, respectively, of heme a3-CO complex based on the 13C18O isotopic frequency shifts. These frequencies are essentially the same as those observed for solubilized cytochrome c oxidase, which implies that the environmental structure of the dioxygen reducing site in the solubilized state is not very much altered. It is likely that the dioxygen reducing reaction studied so far for solubilized enzyme is also valid for intact whole mitochondria." @default.
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• W1991768142 date "2002-05-01" @default.
• W1991768142 modified "2023-09-26" @default.
• W1991768142 title "Resonance Raman Spectra of CytochromecOxidase in Whole Mitochondria" @default.
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• W1991768142 doi "https://doi.org/10.1246/bcsj.75.1001" @default.
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